1bws
From Proteopedia
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CRYSTAL STRUCTURE OF GDP-4-KETO-6-DEOXY-D-MANNOSE EPIMERASE/REDUCTASE FROM ESCHERICHIA COLI A KEY ENZYME IN THE BIOSYNTHESIS OF GDP-L-FUCOSE
Overview
BACKGROUND: The process of guanosine 5'-diphosphate L-fucose, (GDP-L-fucose) biosynthesis is conserved throughout evolution from, prokaryotes to man. In animals, GDP-L-fucose is the substrate of, fucosyltransferases that participate in the biosynthesis and remodeling of, glycoconjugates, including ABH blood group and Lewis-system antigens. The, 'de novo' pathway of GDP-L-fucose biosynthesis from GDP-D-mannose involves, a GDP-D-mannose 4,6 dehydratase (GMD) and a GDP-4-keto-6-deoxy-D-mannose, epimerase/reductase (GMER). Neither of the catalytic mechanisms nor the, three-dimensional structures of the two enzymes has been elucidated yet., The severe leukocyte adhesion deficiency (LAD) type II genetic syndrome is, known to result from deficiencies in this de novo pathway. RESULTS: The, ... [(full description)]
About this Structure
1BWS is a [Single protein] structure of sequence from [Escherichia coli] with NDP as [ligand]. Structure known Active Site: CAT. Full crystallographic information is available from [OCA].
Reference
GDP-4-keto-6-deoxy-D-mannose epimerase/reductase from Escherichia coli, a key enzyme in the biosynthesis of GDP-L-fucose, displays the structural characteristics of the RED protein homology superfamily., Rizzi M, Tonetti M, Vigevani P, Sturla L, Bisso A, Flora AD, Bordo D, Bolognesi M, Structure. 1998 Nov 15;6(11):1453-65. PMID:9817848
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